G01N2333/938

Detection of waterborne pathogens with paper strips
20220348978 · 2022-11-03 ·

The disclosure provides methods and apparatuses to test for E. coli in liquid samples. The apparatus includes a paper strip having a hydrophobic area at one end and a reaction area at the other end.

METHOD FOR ASSESSING THE ABILITY OF A SUBSTANCE OR OF A COMPOSITION TO PREVENT, SLOW OR ELIMINATE THE SIGNS OF AGEING OF THE SKIN OR OF THE LIPS

A method for assessing the ability of a chemical substance or of a chemical composition to prevent or to slow the appearance of signs of aging of the human skin or of the lips or even to eliminate the signs; the method including: —a step a) of bringing the chemical substance or the chemical composition into contact with fibroblast cells of the “young” human dermis taken from a culture medium at the passage R6; —a step b) of bringing senescent cells of fibroblasts of the human dermis into contact with the cells of “young” fibroblasts from step a); and—a step c) of measuring the senescence input of the cells of “young” fibroblasts and of comparing it with a reference value.

MATERIALS AND KITS RELATING TO ASSOCIATION OF REPORTER SPECIES AND TARGETING ENTITIES WITH BEADS
20220205992 · 2022-06-30 · ·

Described herein are materials and kits for associating species with a surface of an object. In some embodiments, the object comprises a plurality of capture objects (e.g., beads).

Prebiotic composition and its methods of production

The present invention relates to a prebiotic composition comprising a galacto oligosaccharide (GOS) produced from Lactobacillus plantarum, wherein the GOS acts as a selective growth medium for a chosen Lactobacillus plantarum probiotic bacterial strain, and wherein the GOS is substantially the same as the form produced by reverse β-galactosidase reaction in the chosen probiotic bacterial strain. The present invention also relates to methods of producing GOS and related composition incorporating the GOS.

Reagents and methods of use with automated analyzers for obtaining a specific gravity index for urine
11214821 · 2022-01-04 · ·

Reagents and methods for using automated laboratory equipment to determine whether the specific gravity of a urine sample is out of normal range as an indication of adulteration. The sodium (Na+) and potassium (K+) normally found in a urine sample can be used as markers. A sodium-potassium dependent β-galactosidase can be utilized with o-nitrophenylgalactoside (o-NPG) which is cleaved into o-nitrophenol, which turns the sample yellow. The sample can be analyzed by spectrophotometry methods utilized in most clinical analyzers at a pre-determined primary wavelength to obtain a Specific gravity Index (SGI). Measurements of the SGI that are outside a known normal range can indicate that the sample integrity has been compromised.

Method of analyzing diluted biological sample component
11808776 · 2023-11-07 · ·

There is provided a method of analyzing a biological sample component that allows easy and accurate quantification and counting of any of a plasma component and a blood cell component in a trace and unknown amount of a whole blood sample collected from a finger, for example. The method of the present invention is a method of analyzing a biological sample component in a trace amount of blood, comprising analyzing a diluent buffer into which the blood has been mixed and an internal standard substance and/or an external standard substance contained in the diluent buffer, calculating a dilution ratio, and analyzing a biological component in a plasma or serum component in the blood.

Method of analyzing diluted biological sample component
11808777 · 2023-11-07 · ·

There is provided a method of analyzing a biological sample component that allows easy and accurate quantification and counting of any of a plasma component and a blood cell component in a trace and unknown amount of a whole blood sample collected from a finger, for example. The method of the present invention is a method of analyzing a biological sample component in a trace amount of blood, comprising analyzing a diluent buffer into which the blood has been mixed and an internal standard substance and/or an external standard substance contained in the diluent buffer, calculating a dilution ratio, and analyzing a biological component in a plasma or serum component in the blood.

METHODS AND ARRAYS FOR TARGET ANALYTE DETECTION AND DETERMINATION OF TARGET ANALYTE CONCENTRATION IN SOLUTION
20220099678 · 2022-03-31 · ·

Arrays of single molecules and methods of producing an array of single molecules are described. Arrays with defined volumes between 10 attoliters and 50 picoliters enable single molecule detection and quantitation.

Methods and arrays for target analyte detection and determination of target analyte concentration in solution

Arrays of single molecules and methods of producing an array of single molecules are described. Arrays with defined volumes between 10 attoliters and 50 picoliters enable single molecule detection and quantitation.

ANTIBODIES HAVING SPECIFICITY FOR THE ORF2I PROTEIN OF HEPATITIS E VIRUS AND USES THEREOF FOR DIAGNOSTIC PURPOSES

Hepatitis E virus (HEV) is annually responsible for 20 million infections with 3.4 million symptomatic cases and 70,000 deaths mainly occurring in less developed regions of the world. HEV is a non-enveloped virus containing a linear, single-stranded, positive-sense RNA genome that contains three open reading frames (ORFs), namely, ORF1, ORF2 and ORF3. ORF2 encodes the ORF2 viral capsid protein, which is involved in particle assembly, binding to host cells and eliciting neutralizing antibodies. Recently, 3 different forms of the ORF2 capsid protein were identified: infectious/intracellular ORF2 (ORF2i), glycosylated ORF2 (ORF2g), and cleaved ORF2 (ORF2c). The ORF2i protein, for which the precise sequence has been identified, is the form that is associated with infectious particles and thus antibodies having specificity for the ORF2i protein would be suitable for the diagnosis of HEV. The present fulfills this need by providing an antibody which binds to the ORF2i protein of hepatitis E virus and wherein said antibody does not bind to the ORF2g protein nor to the ORF2c of hepatitis E virus, and wherein the epitope of said antibody comprises at least one amino acid residue from amino acid residues 542 to 555 of SEQ ID NO: 1.